A heritable switch in carbon source utilization driven by an unusual yeast prion

Brown, Jessica C. S.; Lindquist, Susan

doi:10.1101/gad.1839109

Cited by 162 publications

(224 citation statements)

References 80 publications

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“…This atypical prion causes growth on glycerol in the presence of a nonmetabolizable glucose analog as a dominant non-Mendelian trait. Propagation of [GAR + ] is not dependent upon Hsp104, and the Std1-Pma1 prion complex does not show the characteristics of amyloid (Brown and Lindquist 2009).…”

Section: Prions Of Normal Yeast Proteinsmentioning

confidence: 99%

Prions in Yeast

2012

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The concept of a prion as an infectious self-propagating protein isoform was initially proposed to explain certain mammalian diseases. It is now clear that yeast also has heritable elements transmitted via protein. Indeed, the "protein only" model of prion transmission was first proven using a yeast prion. Typically, known prions are ordered cross-b aggregates (amyloids). Recently, there has been an explosion in the number of recognized prions in yeast. Yeast continues to lead the way in understanding cellular control of prion propagation, prion structure, mechanisms of de novo prion formation, specificity of prion transmission, and the biological roles of prions. This review summarizes what has been learned from yeast prions.

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Section: Prions Of Normal Yeast Proteinsmentioning

confidence: 99%

Prions in Yeast

2012

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“…S3 A-C). Although most known yeast prions are dependent on Hsp104, recently emerging evidence indicates that other molecular chaperones like Hsp70 and, potentially, Hsp90 may play Hsp104-independent roles in prion biology (9,36,37 (Fig. 4A).…”

Section: Identification and Functional Classification Of Arabidopsis mentioning

confidence: 99%

Luminidependens (LD) is an Arabidopsis protein with prion behavior

Chakrabortee

Kayatekin

Newby

et al. 2016

Proc. Natl. Acad. Sci. U.S.A.

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Prion proteins provide a unique mode of biochemical memory through self-perpetuating changes in protein conformation and function. They have been studied in fungi and mammals, but not yet identified in plants. Using a computational model, we identified candidate prion domains (PrDs) in nearly 500 plant proteins. Plant flowering is of particular interest with respect to biological memory, because its regulation involves remembering and integrating previously experienced environmental conditions. We investigated the prion-forming capacity of three prion candidates involved in flowering using a yeast model, where prion attributes are well defined and readily tested. In yeast, prions heritably change protein functions by templating monomers into higherorder assemblies. For most yeast prions, the capacity to convert into a prion resides in a distinct prion domain. Thus, new prionforming domains can be identified by functional complementation of a known prion domain. The prion-like domains (PrDs) of all three of the tested proteins formed higher-order oligomers. Uniquely, the Luminidependens PrD (LDPrD) fully replaced the prion-domain functions of a well-characterized yeast prion, Sup35. Our results suggest that prion-like conformational switches are evolutionarily conserved and might function in a wide variety of normal biological processes.prions | Luminidependens | plant prion domains

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“…They correspond to amyloid forms of Swi1, Mca1, Cyc8, and Mot3 proteins, respectively. Besides these amyloid-based prions, two self-perpetuating determinants of nonamyloid nature, [β] and [GAR + ], were recently described (6,7). Thus, it is evident that protein inheritance is a widespread phenomenon, at least in lower eukaryotes.…”

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Non-Mendelian determinant [ ISP ⁺ ] in yeast is a nuclear-residing prion form of the global transcriptional regulator Sfp1

Rogoza

Goginashvili

Rodionova

et al. 2010

Proc. Natl. Acad. Sci. U.S.A.

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], were recently described (6, 7). Thus, it is evident that protein inheritance is a widespread phenomenon, at least in lower eukaryotes.The discovery of prions in yeast occurred in different ways. Some (i.e., [PSI + ] and [URE3]) were long known as genetic determinants of mysterious nature until their prion nature was proposed (8). The others were revealed by purposeful screening of potentially prionogenic proteins and corresponding determinants. The prion-like determinant [ISP + ], described in our earlier work (9), belongs to the first group, because it was detected as a nonchromosomal antisuppressor in strains containing specific sup35 nonsense suppressor mutations and the nonsense mutations his7-1 (UAA) and lys2-87 (UGA (Fig. 1A). The Sup + phenotype cosegregated with Ura + in tetrads of the diploid that was obtained by crossing the sfp1Δ and [ISP + ] strains (Fig. 1B). These findings indicate either that [ISP + ] is a prion form of Sfp1 or that the change in phenotype was caused by an independent manifestation of the SFP1-null allele.To distinguish between these two possibilities, the sfp1Δ strain was transformed with the centromeric vector pRS315-SFP1. Introduction of the wild-type SFP1 allele did not change the phenotype of the sfp1Δ strain [i.e., the absolute majority (556 of 559) of transformants has retained the Sup + phenotype]. This fact suggests that the change of phenotype in the sfp1Δ strain was caused by [ISP + ] loss rather than phenotypic effects of the SFP1 deletion; otherwise, restoration of the Sup − phenotype would be observed. Notably, this loss was irreversible, because we have not observed a single example of Sup -clones appearing in the mitotic progeny of sfp1Δ strains in contrast to [isp -] strains obtained by GuHCl treatment, which produced Sup -clones at a high frequency (9). These results confirmed that SFP1 could be considered as a likely host gene for [ISP + ].

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A heritable switch in carbon source utilization driven by an unusual yeast prion

Cited by 162 publications

References 80 publications

Prions in Yeast

Prions in Yeast

Luminidependens (LD) is an Arabidopsis protein with prion behavior

Non-Mendelian determinant [ ISP ⁺ ] in yeast is a nuclear-residing prion form of the global transcriptional regulator Sfp1

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A heritable switch in carbon source utilization driven by an unusual yeast prion

Cited by 162 publications

References 80 publications

Prions in Yeast

Prions in Yeast

Luminidependens (LD) is an Arabidopsis protein with prion behavior

Non-Mendelian determinant [ ISP + ] in yeast is a nuclear-residing prion form of the global transcriptional regulator Sfp1

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Product

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About

Non-Mendelian determinant [ ISP ⁺ ] in yeast is a nuclear-residing prion form of the global transcriptional regulator Sfp1